Title

Authors

Affiliation

Department of Biochemistry, Faculty of Medicine & Applied Medical Sciences, Northern Border University, Arar-91431, Saudi Arabia

Email

fsd707@gmail.com; *Corresponding author

Article Type

Hypothesis

Date

Received December 06, 2013; Accepted December 12, 2013; Published December 27, 2013

The β-sheet of muscle fatty acid binding protein of Locusta migratoria (Lm-FABP) was modeled by employing 2-D NMR data and the Rigid Body Assembly method. The model shows the β-sheet to comprise ten β-strands arranged anti-parallel to each other. There is a β-bulge between Ser 13 and Gln 14 which is a difference from the published structure of β-sheet of bovine heart Fatty Acid Binding Protein. Also, a hydrophobic patch consisting of Ile 45, Phe 51, Phe 64 and Phe 66 is present on the surface which is characteristic of most Fatty Acid Binding Proteins. A “gap” is present between βD and βE that provides evidence for the presence of a portal or opening between the polypeptide chains which allows ligand fatty acids to enter the protein cavity and bind to the protein. 

Keywords

Muscle Fatty Acid Binding Protein, Nuclear Overhauser Effect, β-sheet of Lm-FABP, Portal hypothesis, Locusta migratoria.

Citation

Kizilbash et al. Bioinformation 9(20): 1003-1009 (2013)

Edited by

P Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.